Abstract:Inspired by self-assembling peptides found in native proteins, deliberately designed engineered peptides have shown outstanding biocompatibility, biodegradability, and extracellular matrix-mimicking microenvironments. Assembly of the peptides can be triggered by external stimuli, such as electrolytes, temperature, and pH. The formation of nanostructures and subsequent nanocomposite materials often occur under physiological conditions. The respective properties of side chains in each amino acids provide numerou… Show more
“…The intrinsic ability of some peptides to selfassemble into higher order structures allow for numerous applications as functional biomaterials. 330,331 In the last ten years, peptide fibrils caused a paradigm shift in viral gene delivery from using mostly spherical particles to anisotropic, fibrillar nanocarriers, due to their convenient handling and high TE.…”
Therapeutic viral gene delivery is an emerging technology which aims to correct genetic mutations by introducing new genetic information to cells either to correct a faulty gene or to initiate...
“…The intrinsic ability of some peptides to selfassemble into higher order structures allow for numerous applications as functional biomaterials. 330,331 In the last ten years, peptide fibrils caused a paradigm shift in viral gene delivery from using mostly spherical particles to anisotropic, fibrillar nanocarriers, due to their convenient handling and high TE.…”
Therapeutic viral gene delivery is an emerging technology which aims to correct genetic mutations by introducing new genetic information to cells either to correct a faulty gene or to initiate...
“…[1][2][3] Self-assembling peptides, which self-organize from naturally building blocks into supramolecular nanofibrous structures, can be used to recreate native stem cell microenvironments in vivo. 4,5 The initial and rational design for self-assembling peptides was inspired by β-sheet and α-helical structures found in naturally occurring proteins. 2,4,6,7 Insights into peptide folding and intramolecular interactions that drive self-assembly have led to the emergence of customized de novo motifs.…”
By providing a stem cell microenvironment with particular bioactive constituents in vivo, synthetic biomaterials have been progressively successful in stem cell-based tissue regeneration by enhancing the engraftment and survival of transplanted cells. Designs with bioactive motifs to influence cell behavior and with D-form amino acids to modulate scaffold stability may be critical for the development and optimization of self-assembling biomimetic hydrogel scaffolds for stem cell therapy. Materials and Methods: In this study, we linked naphthalene (Nap) covalently to a short D-form peptide (Nap-D F D FG) and the C domain of insulin-like growth factor-1 (IGF-1C) as a functional hydrogel-based scaffolds, and we hypothesized that this hydrogel could enhance the therapeutic efficiency of human placenta-derived mesenchymal stem cells (hP-MSCs) in a murine acute kidney injury (AKI) model. Results: The self-assembling peptide was constrained into a classical β-sheet structure and showed hydrogel properties. Our results revealed that this hydrogel exhibited increased affinity for IGF-1 receptor. Furthermore, cotransplantation of the β-IGF-1C hydrogel and hP-MSCs contributed to endogenous regeneration post-injury and boosted angiogenesis in a murine AKI model, leading to recovery of renal function. Conclusion: This hydrogel could provide a favorable niche for hP-MSCs and thereby rescue renal function in an AKI model by promoting cell survival and angiogenesis. In conclusion, by covalently linking the desired functional groups to D-form peptides to create functional hydrogels, self-assembling β-sheet peptide hydrogels may serve as a promising platform for tissue-engineering and stem cell therapy.
“…π-π stacking between large π-conjugated surfaces provides an overall stability to supramolecular polymers bound together by non-covalent interactions (Cockroft et al, 2005). Various collagen like peptides mimic the fibril formation and assemble into higher order hierarchical structures through π-π stacking interactions (Chen and Zou, 2019). The hypothesis put forward by Gazit et al regarding the lead role played by aromatic interactions in the self-assembly of peptide nanotubes/amyloidlike structures has been established time and again (Reches and Gazit, 2005).…”
Section: Aromatic Interactionsmentioning
confidence: 99%
“…(Kumar et al, 2015;Li I.C. et al, 2016;Moore and Hartgerink, 2017;Lopez-Silva et al, 2018;Chen and Zou, 2019) In a two-component system, in which a porphyrin cap is combined with a cyclic peptide the combination of various binding forces, e.g., hydrogen bonding, metal coordination, and dynamic covalent bonds, allows the delivery of encapsulated ligand (Ozores et al, 2017). These supramolecular injectable biomaterials, that can mimic the natural extracellular matrix nanostructure and show marked cellular infiltration, are ideal scaffolds for tissue engineering strategies.…”
Section: Applications Of Peptide Self-assembliesmentioning
The translational therapies to promote interaction between cell and signal come with stringent eligibility criteria. The chemically defined, hierarchically organized, and simpler yet blessed with robust intermolecular association, the peptides, are privileged to make the cutoff for sensing the cell-signal for biologics delivery and tissue engineering. The signature service and insoluble network formation of the peptide self-assemblies as hydrogels have drawn a spell of research activity among the scientists all around the globe in the past decades. The therapeutic peptide market players are anticipating promising growth opportunities due to the ample technological advancements in this field. The presence of the other organic moieties, enzyme substrates and well-established protecting groups like Fmoc and Boc etc., bring the best of both worlds. Since the large sequences of peptides severely limit the purification and their isolation, this article reviews the account of last 5 years' efforts on novel approaches for formulation and development of single molecule amino acids, ultra-short peptide self-assemblies (di-and tri-peptides only) and their derivatives as drug/gene carriers and tissue-engineering systems.
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